POP4_YEAST
ID POP4_YEAST Reviewed; 279 AA.
AC P38336; D6VQQ4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=RNases MRP/P 32.9 kDa subunit;
DE AltName: Full=RNA-processing protein POP4;
GN Name=POP4; OrderedLocusNames=YBR257W; ORFNames=YBR1725;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8465606; DOI=10.1002/yea.320090210;
RA Doignon F., Biteau N., Crouzet M., Aigle M.;
RT "The complete sequence of a 19,482 bp segment located on the right arm of
RT chromosome II from Saccharomyces cerevisiae.";
RL Yeast 9:189-199(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9085845;
RA Chu S., Zengel J.M., Lindahl L.;
RT "A novel protein shared by RNase MRP and RNase P.";
RL RNA 3:382-391(1997).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN THE RNASE P COMPLEX BY MASS SPECTROMETRY.
RX PubMed=9620854; DOI=10.1101/gad.12.11.1678;
RA Chamberlain J.R., Lee Y., Lane W.S., Engelke D.R.;
RT "Purification and characterization of the nuclear RNase P holoenzyme
RT complex reveals extensive subunit overlap with RNase MRP.";
RL Genes Dev. 12:1678-1690(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [7]
RP IDENTIFICATION IN THE RNASE MRP COMPLEX BY MASS SPECTROMETRY.
RX PubMed=15637077; DOI=10.1074/jbc.m409568200;
RA Salinas K., Wierzbicki S., Zhou L., Schmitt M.E.;
RT "Characterization and purification of Saccharomyces cerevisiae RNase MRP
RT reveals a new unique protein component.";
RL J. Biol. Chem. 280:11352-11360(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Required for 5.8S rRNA and tRNA processing; associated with
CC RNase MRP and RNase P. {ECO:0000269|PubMed:9085845,
CC ECO:0000269|PubMed:9620854}.
CC -!- SUBUNIT: Component of nuclear RNase P and RNase MRP complexes. RNase P
CC consists of an RNA moiety and at least 9 protein subunits including
CC POP1, POP3, POP4, POP5, POP6, POP7, POP8, RPP1 and RPR2. RNase MRP
CC complex consists of an RNA moiety and at least 10 protein subunits
CC including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RMP1, RPP1 and
CC SNM1, many of which are shared with the RNase P complex.
CC {ECO:0000269|PubMed:15637077, ECO:0000269|PubMed:9085845,
CC ECO:0000269|PubMed:9620854}.
CC -!- INTERACTION:
CC P38336; P41812: POP1; NbExp=5; IntAct=EBI-13646, EBI-13621;
CC P38336; P53218: POP6; NbExp=4; IntAct=EBI-13646, EBI-13662;
CC P38336; P38291: POP7; NbExp=3; IntAct=EBI-13646, EBI-13670;
CC P38336; P38786: RPP1; NbExp=3; IntAct=EBI-13646, EBI-15968;
CC P38336; P40571: RPR2; NbExp=3; IntAct=EBI-13646, EBI-25408;
CC P38336; P40993: SNM1; NbExp=4; IntAct=EBI-13646, EBI-15622;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X70529; CAA49921.1; -; Genomic_DNA.
DR EMBL; Z36126; CAA85220.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07374.1; -; Genomic_DNA.
DR PIR; S32959; S32959.
DR RefSeq; NP_009816.1; NM_001178605.1.
DR PDB; 6AGB; EM; 3.48 A; D=1-279.
DR PDB; 6AH3; EM; 3.48 A; D=1-279.
DR PDB; 6W6V; EM; 3.00 A; D=1-279.
DR PDB; 7C79; EM; 2.50 A; D=1-279.
DR PDB; 7C7A; EM; 2.80 A; D=1-279.
DR PDBsum; 6AGB; -.
DR PDBsum; 6AH3; -.
DR PDBsum; 6W6V; -.
DR PDBsum; 7C79; -.
DR PDBsum; 7C7A; -.
DR AlphaFoldDB; P38336; -.
DR SMR; P38336; -.
DR BioGRID; 32953; 294.
DR ComplexPortal; CPX-1873; Nucleolar ribonuclease P complex.
DR ComplexPortal; CPX-3284; Nucleolar ribonuclease MRP complex.
DR DIP; DIP-6772N; -.
DR IntAct; P38336; 10.
DR MINT; P38336; -.
DR STRING; 4932.YBR257W; -.
DR iPTMnet; P38336; -.
DR MaxQB; P38336; -.
DR PaxDb; P38336; -.
DR PRIDE; P38336; -.
DR EnsemblFungi; YBR257W_mRNA; YBR257W; YBR257W.
DR GeneID; 852560; -.
DR KEGG; sce:YBR257W; -.
DR SGD; S000000461; POP4.
DR VEuPathDB; FungiDB:YBR257W; -.
DR eggNOG; KOG4046; Eukaryota.
DR GeneTree; ENSGT00390000010067; -.
DR HOGENOM; CLU_998037_0_0_1; -.
DR InParanoid; P38336; -.
DR OMA; RFKYRSS; -.
DR BioCyc; YEAST:G3O-29181-MON; -.
DR PRO; PR:P38336; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38336; protein.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IDA:SGD.
DR GO; GO:0000172; C:ribonuclease MRP complex; IDA:SGD.
DR GO; GO:0030677; C:ribonuclease P complex; IDA:SGD.
DR GO; GO:0033204; F:ribonuclease P RNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:SGD.
DR GO; GO:0034965; P:intronic box C/D RNA processing; IDA:SGD.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IDA:ComplexPortal.
DR GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; IDA:SGD.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IEA:GOC.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:ComplexPortal.
DR GO; GO:0008033; P:tRNA processing; IMP:SGD.
DR Gene3D; 2.30.30.210; -; 1.
DR InterPro; IPR016848; RNase_P/MRP_Rpp29-subunit.
DR InterPro; IPR036980; RNase_P/MRP_Rpp29_sf.
DR InterPro; IPR023534; Rof/RNase_P-like.
DR InterPro; IPR002730; Rpp29/RNP1.
DR PANTHER; PTHR13348; PTHR13348; 1.
DR Pfam; PF01868; RNase_P-MRP_p29; 1.
DR PIRSF; PIRSF027081; RNase_P/MRP_p29_subunit; 1.
DR SMART; SM00538; POP4; 1.
DR SUPFAM; SSF101744; SSF101744; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; rRNA processing;
KW tRNA processing.
FT CHAIN 1..279
FT /note="RNases MRP/P 32.9 kDa subunit"
FT /id="PRO_0000128422"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 69..109
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 136..154
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:7C7A"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6W6V"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:7C7A"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:6W6V"
FT HELIX 274..278
FT /evidence="ECO:0007829|PDB:7C79"
SQ SEQUENCE 279 AA; 32881 MW; F19FD05B47DE83C1 CRC64;
MDRTQTFIKD CLFTKCLEDP EKPFNENRFQ DTLLLLPTDG GLTSRLQRQQ RKSKLNLDNL
QKVSQLESAD KQLEKRDYQR INKNSKIALR EYINNCKKNT KKCLKLAYEN KITDKEDLLH
YIEEKHPTIY ESLPQYVDFV PMYKELWINY IKELLNITKN LKTFNGSLAL LKLSMADYNG
ALLRVTKSKN KTLIGLQGIV IWDSQKFFIM IVKGNIIDEI KCIPKKGTVF QFEIPISDDD
DSALRYSILG DRFKYRSVDR AGRKFKSRRC DDMLYYIQN
